Henry F. Epstein, M.D.,
Professor

Henry F. Epstein, M.D.

About the Lab

Dr. Epstein's laboratory is studying the role of chaperone-mediated folding in regulatory mechanisms of development and disease.

Biochemical and genetic studies on the C. elegans model as well as in various fungal species have demonstrated that a novel molecular chaperone is required for the proper folding, assembly, and function of myosins and myosin-like protein motors. The chaperone protein, named UNC-45 after the canonical gene in C. elegans, binds the well-known molecular chaperone Hsp90 as well as myosin. In mice and humans, two UNC-45-like genes are present and encode closely related but distinct isoforms. One isoform is present in many cell types and appears necessary for cell division and membrane fusion; the other isoform is expressed predominantly in heart and skeletal muscle and is necessry for sarcomere organization. The UNC-45 mammalian homologues may prove to be important targets for genetic and pharmacological intervention in certain cancers and heart failure.

Book Chapters:

Singh, Ram and Epstein, H.F. Biochemistry of myotonic dystrophy protein kinase (DMPK), In Genetic Instabilities and Neurological Diseases 2nd edition (Editors Tetsuo Ashizawa and Robert D. Wells), Elsevier, San Diego, USA, Chapter 6, pp.99-113, 2006.

Odunuga, O.O., and Epstein HF. UNC-45: a chaperone for myosin and a co-chaperone for Hsp90. In: Networking of Chaperones by Co-chaperones, (Editor GL Blatch GL). Landes Bioscience, Georgetown, Texas, USA, 2006.

Reviews:

Hutagalung, A.H., Landsverk, M.L., Price, M.G. and Epstein, H.F.  The UCS family of myosin chaperones.  J. Cell  Sci., 115:398-3990, 2002.

Landsverk M.L. and Epstein H.F. Genetic analysis of myosin II assembly and organization in model organisms. Cell Mol Life Sci., 62: 2270-82, 2005

Link to my publications on pubmed (in addition to the one on the sidebar):

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